| Host: |
HEK293 cells |
| Reactivity: |
Human |
| Note: |
STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS. |
| Short Description: |
Recombinant-Human Microtubule-associated protein tau/MAPT-C-His protein was developed from hek293 cells and has a target region of C-His. For use in research applications. |
| Formulation: |
Lyophilized from a 0.22 Mu m filtered solution of PBS, pH 7.4. |
| Gene Symbol: |
MAPT |
| Gene ID: |
4137 |
| Uniprot ID: |
TAU_HUMAN |
| Immunogen: |
Recombinant Human Microtubule-associated protein tau/MAPT Protein is produced by HEK293 cells expression system. The target protein is expressed with sequence (Met1-Leu441) of human Tau-F/MAPT-F (Accession #NP_005901.2) fused with a 6×His tag at the |
| Post Translational Modifications | Phosphorylation at serine and threonine residues in S-P or T-P motifs by proline-directed protein kinases (PDPK1, CDK1, CDK5, GSK3, MAPK) (only 2-3 sites per protein in interphase, seven-fold increase in mitosis, and in the form associated with paired helical filaments (PHF-tau)), and at serine residues in K-X-G-S motifs by MAP/microtubule affinity-regulating kinase (MARK1, MARK2, MARK3 or MARK4), causing detachment from microtubules, and their disassembly. Phosphorylation decreases with age. Phosphorylation within tau/MAP's repeat domain or in flanking regions seems to reduce tau/MAP's interaction with, respectively, microtubules or plasma membrane components. Phosphorylation on Ser-610, Ser-622, Ser-641 and Ser-673 in several isoforms during mitosis. Phosphorylation at Ser-548 by GSK3B reduces ability to bind and stabilize microtubules. Phosphorylation at Ser-579 by BRSK1 and BRSK2 in neurons affects ability to bind microtubules and plays a role in neuron polarization. Phosphorylated at Ser-554, Ser-579, Ser-602, Ser-606 and Ser-669 by PHK. Phosphorylation at Ser-214 by SGK1 mediates microtubule depolymerization and neurite formation in hippocampal neurons. There is a reciprocal down-regulation of phosphorylation and O-GlcNAcylation. Phosphorylation on Ser-717 completely abolishes the O-GlcNAcylation on this site, while phosphorylation on Ser-713 and Ser-721 reduces glycosylation by a factor of 2 and 4 respectively. Phosphorylation on Ser-721 is reduced by about 41.5% by GlcNAcylation on Ser-717. Dephosphorylated at several serine and threonine residues by the serine/threonine phosphatase PPP5C. Polyubiquitinated. Requires functional TRAF6 and may provoke SQSTM1-dependent degradation by the proteasome. PHF-tau can be modified by three different forms of polyubiquitination. 'Lys-48'-linked polyubiquitination is the major form, 'Lys-6'-linked and 'Lys-11'-linked polyubiquitination also occur. O-glycosylated. O-GlcNAcylation content is around 8.2%. There is reciprocal down-regulation of phosphorylation and O-GlcNAcylation. Phosphorylation on Ser-717 completely abolishes the O-GlcNAcylation on this site, while phosphorylation on Ser-713 and Ser-721 reduces O-GlcNAcylation by a factor of 2 and 4 respectively. O-GlcNAcylation on Ser-717 decreases the phosphorylation on Ser-721 by about 41.5%. Glycation of PHF-tau, but not normal brain TAU/MAPT. Glycation is a non-enzymatic post-translational modification that involves a covalent linkage between a sugar and an amino group of a protein molecule forming ketoamine. Subsequent oxidation, fragmentation and/or cross-linking of ketoamine leads to the production of advanced glycation endproducts (AGES). Glycation may play a role in stabilizing PHF aggregation leading to tangle formation in AD. |
| Function | Promotes microtubule assembly and stability, and might be involved in the establishment and maintenance of neuronal polarity. The C-terminus binds axonal microtubules while the N-terminus binds neural plasma membrane components, suggesting that tau functions as a linker protein between both. Axonal polarity is predetermined by TAU/MAPT localization (in the neuronal cell) in the domain of the cell body defined by the centrosome. The short isoforms allow plasticity of the cytoskeleton whereas the longer isoforms may preferentially play a role in its stabilization. |
| Protein Name | Microtubule-Associated Protein TauNeurofibrillary Tangle ProteinPaired Helical Filament-TauPhf-Tau |
| Database Links | Reactome: R-HSA-264870Reactome: R-HSA-9619483 P10636-8 |
| Cellular Localisation | CytoplasmCytosolCell MembranePeripheral Membrane ProteinCytoplasmic SideCytoskeletonCell ProjectionAxonDendriteSecretedMostly Found In The Axons Of NeuronsIn The Cytosol And In Association With Plasma Membrane ComponentsCan Be SecretedThe Secretion Is Dependent On Protein Unfolding And Facilitated By The Cargo Receptor Tmed10It Results In Protein Translocation From The Cytoplasm Into The Ergic (Endoplasmic Reticulum-Golgi Intermediate Compartment) Followed By Vesicle Entry And Secretion |
| Alternative Protein Names | Microtubule-Associated Protein Tau proteinNeurofibrillary Tangle Protein proteinPaired Helical Filament-Tau proteinPhf-Tau proteinMAPT proteinMAPTL proteinMTBT1 proteinTAU protein |
Information sourced from Uniprot.org
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